Words similar to fibrillin
Example sentences for: fibrillin
How can you use “fibrillin” in a sentence? Here are some example sentences to help you improve your vocabulary:
The deposition of newly synthesized fibrillin into the matrix was greatly reduced (13 % of normal), however, suggesting that the internally deleted mutant fibrillin-1 molecules are secreted and exert a dominant-negative effect on extracellular microfibril assembly.
It is well established that EGF-like modules are important structural features found in many extracellular proteins and that these modules enable numerous protein :protein interactions; the binding of EGF-like modules in laminin to nidogen [ 19 ] and the interaction of EGF-like modules within fibrillin monomers [ 20 21 ] . Calcium may be required for some of these protein interactions.
Each has a signal sequence (55 amino acids and 49, respectively), a second domain containing an EGF-like repeat, a proline/glycine rich region, a fibrillin motif [ 17 ] , an EGF calcium-binding repeat, and a TGF-β repeat (390 and 389 amino acids, respectively), a third domain containing a proline/glycine rich region (113 and 111 amino acids, respectively), a fourth domain containing numerous calcium-binding type II EGF-like modules (D/N)(I/V)(D/N)(E/D)C 1 (678 and 677 amino acids, respectively) and a fifth carboxyl-terminal domain (5 and 21 amino acids, respectively) (human LTBP-3 information was obtained from the GenBank database accession no.
Primary fibroblast cultures from patients and control individuals were grown to confluency and then metabolically labeled with 35S-cysteine as described [ 17 18 ] . The soluble cell lysis fraction, containing newly synthesized labeled fibrillin-1 molecules, and the insoluble fraction, representing the labeled fibrillin in the extracellular matrix, were fractionated by SDS polyacrylamide gel electrophoresis and autoradiographed.
3. In addition, we found that certain cysteine substitutions in EGF-like domains and located immediately N-terminal of LTBP-like domains, cause protein instability and greatly reduced matrix deposition [ 9 ] . Taken together, our data support a model in which misfolding or partial deletion of LTBP-like domains results in proteolytic cleavage of the mutant fibrillin molecules.
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